A personal account on 25 years of scientific literature on [FeFe]-hydrogenase

[FeFe]-hydrogenases are gas-processing metalloenzymes that catalyze H-2 oxidation and proton reduction (H-2 release) in microorganisms. Their high turnover frequencies and lack of electrical overpotential in the hydrogen conversion reaction has inspired generations of biologists, chemists, and physicists to explore the inner workings of [FeFe]-hydrogenase. Here, we revisit 25 years of scientific literature on [FeFe]-hydrogenase and propose a personal account on 'must-read' research papers and review article that will allow interested scientists to follow the recent discussions on catalytic mechanism, O-2 sensitivity, and the in vivo synthesis of the active site cofactor with its biologically uncommon ligands carbon monoxide and cyanide. Focused on-but not restricted to-structural biology and molecular biophysics, we highlight future directions that may inspire young investigators to pursue a career in the exciting and competitive field of [FeFe]-hydrogenase research.

Automated summary

This article reviews 25 years of scientific literature on [FeFe]-hydrogenase and provides a personal account on essential research papers and review articles regarding catalytic mechanism, O-2 sensitivity, and the in vivo synthesis of the active site cofactor. It also highlights future directions in structural biology and molecular biophysics and aims to inspire young investigators in the competitive field of [FeFe]-hydrogenase research.